Computational analysis of chain flexibility and fluctuations in Rhizomucor miehei lipase
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چکیده
منابع مشابه
Immobilization of Rhizomucor miehei Lipase on High Density Polyethylene
Immobilization of Lipase produced from Rhizomucor miehei on HDPE fine powder was investigated. As compared to an aqueous system, immobilization in a non-aquous organic medium such as n-hexane was not successful and caused enzyme denaturation. Prewetting the support with ethanol increased the immobilized protein and enzyme activity as much as 31% and 34%, respectively. The maximum immobilized a...
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To improve the performance of yeast surface-displayed Rhizomucor miehei lipase (RML) in the production of human milk fat substitute (HMFS), we mutated amino acids in the lipase substrate-binding pocket based on protein hydrophobicity, to improve esterification activity. Five mutants: Asn87Ile, Asn87Ile/Asp91Val, His108Leu/Lys109Ile, Asp256Ile/His257Leu, and His108Leu/Lys109Ile/Asp256Ile/His257L...
متن کاملEnantioselectivity of recombinant Rhizomucor miehei lipase in the ring opening of oxazolin-5(4H)-ones.
Enantioselectivity of enzyme catalysis is often rationalized via active site models. These models are constructed on the basis of comparing the enantiomeric excess of product observed in a series of reactions which are conducted with a range of homologous substrates, typically carrying various side chain substitutions. Surprisingly the practical application of these simple but informative 'pock...
متن کاملEnantioselective transacetylation of (R,S)-β-citronellol by propanol rinsed immobilized Rhizomucor miehei lipase
BACKGROUND Use of enzymes in low water media is now widely used for synthesis and kinetic resolution of organic compounds. The frequently used enzyme form is the freeze-dried powders. It has been shown earlier that removal of water molecules from enzyme by rinsing with n-propanol gives preparation (PREP) which show higher activity in low water media. The present work evaluates PREP of the lipas...
متن کاملRole of an electrostatic network of residues in the enzymatic action of the Rhizomucor miehei lipase family.
We have used continuum electrostatic methods to investigate the role of electrostatic interactions in the structure, function, and pH-dependent stability of the fungal Rhizomucor miehei lipase (RmL) family. We identify a functionally important electrostatic network which includes residues S144, D203, H257, Y260, H143, Y28, R80, and D91 (residue numbering is from RmL). This network consists of r...
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ژورنال
عنوان ژورنال: Protein Engineering, Design and Selection
سال: 1999
ISSN: 1741-0134,1741-0126
DOI: 10.1093/protein/12.9.747